RS3A_DROME
ID RS3A_DROME Reviewed; 268 AA.
AC P55830; C4IXY1; E4NKK4; H0RNB6; H9XVL9; O44389; Q8IMA9; Q8IMB0; Q8SZD2;
AC Q9V4A9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=40S ribosomal protein S3a {ECO:0000255|HAMAP-Rule:MF_03122};
DE AltName: Full=C3 protein;
GN Name=RpS3A {ECO:0000255|HAMAP-Rule:MF_03122}; Synonyms=C3, M(4)101;
GN ORFNames=CG2168;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=9393444; DOI=10.1007/s004380050590;
RA Reynaud E., Bolshakov V.N., Barajas V.N., Kafatos F.C., Zurita M.;
RT "Antisense suppression of the putative ribosomal protein S3A gene disrupts
RT ovarian development in Drosophila melanogaster.";
RL Mol. Gen. Genet. 256:462-467(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND DEVELOPMENTAL STAGE.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=9742251; DOI=10.1093/nar/26.19.4471;
RA van Beest M., Mortin M., Clevers H.;
RT "Drosophila RpS3a, a novel minute gene situated between the segment
RT polarity genes cubitus interruptus and dTCF.";
RL Nucleic Acids Res. 26:4471-4475(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- FUNCTION: Essential for oogenesis; required for late follicle cell
CC development. {ECO:0000255|HAMAP-Rule:MF_03122,
CC ECO:0000269|PubMed:9393444}.
CC -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC contains about 33 different proteins and 1 molecule of RNA (18S). The
CC 60S subunit contains about 49 different proteins and 3 molecules of RNA
CC (28S, 5.8S and 5S). {ECO:0000255|HAMAP-Rule:MF_03122}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122,
CC ECO:0000269|PubMed:9393444}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=2;
CC Name=A; Synonyms=F;
CC IsoId=P55830-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P55830-2; Sequence=VSP_038423;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in stage 8 embryos. During
CC oogenesis, expression is located basally in somatic follicular
CC epithelium and in the oocyte at the later stages.
CC {ECO:0000269|PubMed:9393444}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout all development. {ECO:0000269|PubMed:9742251}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit disappearance of the follicular
CC cells of the ovary and abnormalities of the associated germline
CC derivatives, leading to failure of egg production.
CC {ECO:0000269|PubMed:9393444}.
CC -!- MISCELLANEOUS: [Isoform B]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03122}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48571.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ACQ89821.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ADR66775.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AEU08331.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y10115; CAA71201.1; -; mRNA.
DR EMBL; AF034971; AAC62117.1; -; mRNA.
DR EMBL; AE014135; AAF59372.1; -; Genomic_DNA.
DR EMBL; AE014135; AAN06541.1; -; Genomic_DNA.
DR EMBL; AE014135; AFH06764.1; -; Genomic_DNA.
DR EMBL; AY070949; AAL48571.1; ALT_FRAME; mRNA.
DR EMBL; BT083412; ACQ89821.1; ALT_INIT; mRNA.
DR EMBL; BT125801; ADR66775.1; ALT_INIT; mRNA.
DR EMBL; BT132838; AEU08331.1; ALT_INIT; mRNA.
DR RefSeq; NP_001245404.1; NM_001258475.2. [P55830-1]
DR RefSeq; NP_524618.1; NM_079879.4. [P55830-1]
DR RefSeq; NP_726518.1; NM_166714.4. [P55830-2]
DR PDB; 4V6W; EM; 6.00 A; AB=1-268.
DR PDB; 6XU6; EM; 3.50 A; AB=17-236.
DR PDB; 6XU7; EM; 4.90 A; AB=17-236.
DR PDB; 6XU8; EM; 3.00 A; AB=17-236.
DR PDBsum; 4V6W; -.
DR PDBsum; 6XU6; -.
DR PDBsum; 6XU7; -.
DR PDBsum; 6XU8; -.
DR AlphaFoldDB; P55830; -.
DR SMR; P55830; -.
DR BioGRID; 68606; 122.
DR IntAct; P55830; 3.
DR MINT; P55830; -.
DR STRING; 7227.FBpp0300615; -.
DR PaxDb; P55830; -.
DR PRIDE; P55830; -.
DR DNASU; 43768; -.
DR EnsemblMetazoa; FBtr0089175; FBpp0088242; FBgn0017545. [P55830-1]
DR EnsemblMetazoa; FBtr0089176; FBpp0088243; FBgn0017545. [P55830-2]
DR EnsemblMetazoa; FBtr0308296; FBpp0300615; FBgn0017545. [P55830-1]
DR GeneID; 43768; -.
DR KEGG; dme:Dmel_CG2168; -.
DR UCSC; CG2168-RB; d. melanogaster.
DR UCSC; CG2168-RD; d. melanogaster.
DR CTD; 6189; -.
DR FlyBase; FBgn0017545; RpS3A.
DR VEuPathDB; VectorBase:FBgn0017545; -.
DR eggNOG; KOG1628; Eukaryota.
DR GeneTree; ENSGT00390000018433; -.
DR HOGENOM; CLU_062507_0_1_1; -.
DR InParanoid; P55830; -.
DR OMA; GQNAYTK; -.
DR PhylomeDB; P55830; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-DME-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-DME-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-DME-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 43768; 1 hit in 1 CRISPR screen.
DR ChiTaRS; RpS3A; fly.
DR GenomeRNAi; 43768; -.
DR PRO; PR:P55830; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0017545; Expressed in eye disc (Drosophila) and 24 other tissues.
DR Genevisible; P55830; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; TAS:FlyBase.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR HAMAP; MF_03122; Ribosomal_S3Ae_euk; 1.
DR InterPro; IPR027500; Ribosomal_S1/3_euk.
DR InterPro; IPR001593; Ribosomal_S3Ae.
DR InterPro; IPR018281; Ribosomal_S3Ae_CS.
DR Pfam; PF01015; Ribosomal_S3Ae; 1.
DR SMART; SM01397; Ribosomal_S3Ae; 1.
DR PROSITE; PS01191; RIBOSOMAL_S3AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; Cytoplasm;
KW Developmental protein; Differentiation; Oogenesis; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03122"
FT CHAIN 2..268
FT /note="40S ribosomal protein S3a"
FT /id="PRO_0000153529"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..63
FT /note="MAVGKNKGLSKGGKKGGKKKVVDPFSRKDWYDVKAPNMFQTRQIGKTLVNRT
FT QGQRIASDYLK -> MSKLRICFKPVKS (in isoform B)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_038423"
FT CONFLICT 62
FT /note="L -> F (in Ref. 1; CAA71201)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="A -> VP (in Ref. 1; CAA71201)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="R -> H (in Ref. 1; CAA71201)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="S -> C (in Ref. 6; ADR66775)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..161
FT /note="QQ -> HE (in Ref. 1; CAA71201)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="A -> SG (in Ref. 1; CAA71201)"
FT /evidence="ECO:0000305"
FT CONFLICT 253..261
FT /note="VIDRPEGYE -> PKSTALKVK (in Ref. 1; CAA71201)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="A -> S (in Ref. 1; CAA71201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 30340 MW; EA407157F81955C6 CRC64;
MAVGKNKGLS KGGKKGGKKK VVDPFSRKDW YDVKAPNMFQ TRQIGKTLVN RTQGQRIASD
YLKGRVFEVS LADLQKDIDP ERSFRKFRLI AEDVQDRNVL CNFHGMDLTT DKYRSMVKKW
QTLIEAIVEA KTVDGYLLRV FCIGFTAKDQ QSQRKTCYAQ QSQVRKIRAR MTDIITNEVS
GADLKQLVNK LALDSIAKDI EKSCQRIYPL HDVYIRKVKV LKKPRFDVSK LLELHGDGGG
KSVEAVVSSE GAVIDRPEGY EPPVQEAV
